+Open data
-Basic information
Entry | Database: PDB / ID: 2nq8 | ||||||
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Title | Malarial enoyl acyl ACP reductase bound with INH-NAD adduct | ||||||
Components | (Enoyl-acyl carrier reductase) x 2 | ||||||
Keywords | OXIDOREDUCTASE / PfENR / INH / malaria | ||||||
Function / homology | Function and homology information enoyl-[acyl-carrier-protein] reductase (NADH) activity / fatty acid biosynthetic process / nucleotide binding Similarity search - Function | ||||||
Biological species | Plasmodium falciparum (malaria parasite P. falciparum) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2.5 Å | ||||||
Authors | Freundlich, J.S. / Yu, M. / Lucumi, E. / Kuo, M. / Tsai, H.C. / Valderramos, J.C. / Karagyozov, L. / Jacobs Jr., W.R. / Schiehser, G.A. / Fidock, D.A. ...Freundlich, J.S. / Yu, M. / Lucumi, E. / Kuo, M. / Tsai, H.C. / Valderramos, J.C. / Karagyozov, L. / Jacobs Jr., W.R. / Schiehser, G.A. / Fidock, D.A. / Jacobus, D.P. / Sacchettini, J.C. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2007 Title: X-ray structural analysis of Plasmodium falciparum enoyl acyl carrier protein reductase as a pathway toward the optimization of triclosan antimalarial efficacy Authors: Freundlich, J.S. / Wang, F. / Tsai, H.C. / Kuo, M. / Shieh, H.M. / Anderson, J.W. / Nkrumah, L.J. / Valderramos, J.C. / Yu, M. / Kumar, T.R. / Valderramos, S.G. / Jacobs, W.R. / Schiehser, G. ...Authors: Freundlich, J.S. / Wang, F. / Tsai, H.C. / Kuo, M. / Shieh, H.M. / Anderson, J.W. / Nkrumah, L.J. / Valderramos, J.C. / Yu, M. / Kumar, T.R. / Valderramos, S.G. / Jacobs, W.R. / Schiehser, G.A. / Jacobus, D.P. / Fidock, D.A. / Sacchettini, J.C. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2nq8.cif.gz | 131.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2nq8.ent.gz | 102.9 KB | Display | PDB format |
PDBx/mmJSON format | 2nq8.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/nq/2nq8 ftp://data.pdbj.org/pub/pdb/validation_reports/nq/2nq8 | HTTPS FTP |
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-Related structure data
Related structure data | 2foiC 2ol4C 2oosC 2op0C 2op1C 1nhd S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Details | The biological assembly is a teramer generated from the dimer in the asymmetric unit |
-Components
#1: Protein | Mass: 25744.570 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Plasmodium falciparum (malaria parasite P. falciparum) Gene: FabI / Production host: Escherichia coli (E. coli) / References: UniProt: Q9BH77, UniProt: Q9BJJ9*PLUS #2: Protein | Mass: 6829.676 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Plasmodium falciparum (malaria parasite P. falciparum) Gene: FabI / Production host: Escherichia coli (E. coli) / References: UniProt: Q9BH77 #3: Chemical | #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.76 Å3/Da / Density % sol: 55.51 % |
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Crystal grow | Temperature: 289 K / Method: vapor diffusion, hanging drop / pH: 5.6 Details: 2.4M (NH4)2SO4, 0.1M MES ( PH 5.6), VAPOR DIFFUSION, HANGING DROP, temperature 289K |
-Data collection
Diffraction | Mean temperature: 121 K |
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Diffraction source | Source: ROTATING ANODE / Type: BRUKER AXS MICROSTAR / Wavelength: 1.5418 Å |
Detector | Type: BRUKER SMART 2000 / Detector: CCD |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.5→70.15 Å / Num. all: 25925 / Num. obs: 24589 / % possible obs: 94.8 % / Observed criterion σ(I): 1 |
Reflection shell | Resolution: 2.5→2.63 Å / Redundancy: 15.18 % / Rmerge(I) obs: 0.274 / Mean I/σ(I) obs: 0.71 / Num. unique all: 3280 / Rsym value: 0.277 / % possible all: 99.76 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1NHD 1nhd Resolution: 2.5→70.15 Å / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Displacement parameters | Biso mean: 39.9 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.5→70.15 Å
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Refine LS restraints |
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